Detail Information for IndEnz0002009292
IED ID IndEnz0002009292
Enzyme Type ID protease009292
Protein Name Ovalbumin
Allergen Gal d II
Egg albumin
Plakalbumin
allergen Gal d 2
Gene Name SERPINB14
Organism Gallus gallus (Chicken)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Sauropsida Sauria (diapsids) Archelosauria Archosauria Dinosauria Saurischia Theropoda Coelurosauria Aves Neognathae Galloanserae Galliformes Phasianidae (turkeys) Phasianinae Gallus Gallus gallus (Chicken)
Enzyme Sequence MGSIGAASMEFCFDVFKELKVHHANENIFYCPIAIMSALAMVYLGAKDSTRTQINKVVRFDKLPGFGDSIEAQCGTSVNVHSSLRDILNQITKPNDVYSFSLASRLYAEERYPILPEYLQCVKELYRGGLEPINFQTAADQARELINSWVESQTNGIIRNVLQPSSVDSQTAMVLVNAIVFKGLWEKAFKDEDTQAMPFRVTEQESKPVQMMYQIGLFRVASMASEKMKILELPFASGTMSMLVLLPDEVSGLEQLESIINFEKLTEWTSSNVMEERKIKVYLPRMKMEEKYNLTSVLMAMGITDVFSSSANLSGISSAESLKISQAVHAAHAEINEAGREVVGSAEAGVDAASVSEEFRADHPFLFCIKHIATNAVLFFGRCVSP
Enzyme Length 386
Uniprot Accession Number P01012
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: Non-inhibitory serpin. Storage protein of egg white. {ECO:0000269|PubMed:3732511, ECO:0000269|PubMed:6749856}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (17); Chain (1); Disulfide bond (1); Glycosylation (1); Helix (14); Initiator methionine (1); Metal binding (1); Modified residue (3); Mutagenesis (3); Natural variant (2); Sequence conflict (3); Signal peptide (1); Site (2); Turn (9)
Keywords 3D-structure;Acetylation;Allergen;Calcium;Direct protein sequencing;Disulfide bond;Glycoprotein;Metal-binding;Phosphoprotein;Reference proteome;Secreted;Signal
Interact With
Induction INDUCTION: Down-regulated by dietary stress. Decreased expression at day 14 in the magnum of the oviduct in the corticosterone-fed laying hens. {ECO:0000269|PubMed:25436390}.
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6749856}.
Modified Residue MOD_RES 2; /note="N-acetylglycine"; /evidence="ECO:0000269|PubMed:272676, ECO:0000269|PubMed:751625"; MOD_RES 69; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:6783411"; MOD_RES 345; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:6783411"
Post Translational Modification PTM: Undergoes proteolytic cleavage first at the canonical P1-P1' site, and then at the P8-P7 site by subtilisin. {ECO:0000269|PubMed:11779232, ECO:0000269|PubMed:11931671}.
Signal Peptide SIGNAL 22..48; /note=Not cleaved
Structure 3D X-ray crystallography (12)
Cross Reference PDB 1JTI; 1OVA; 1P1Z; 1P4L; 1UHG; 1VAC; 3C8K; 3CVH; 3P9L; 3P9M; 3PAB; 4HKJ;
Mapped Pubmed ID 12840013; 14595439; 18426793; 18703505; 22039305; 23209377; 26312056; 7708669;
Motif
Gene Encoded By
Mass 42,881
Kinetics
Metal Binding METAL 192; /note=Calcium
Rhea ID
Cross Reference Brenda